MSRP_SERP5
ID MSRP_SERP5 Reviewed; 333 AA.
AC A8GK68;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Protein-methionine-sulfoxide reductase catalytic subunit MsrP {ECO:0000255|HAMAP-Rule:MF_01206};
DE EC=1.8.5.- {ECO:0000255|HAMAP-Rule:MF_01206};
DE Flags: Precursor;
GN Name=msrP {ECO:0000255|HAMAP-Rule:MF_01206}; OrderedLocusNames=Spro_4414;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the MsrPQ system that repairs oxidized periplasmic
CC proteins containing methionine sulfoxide residues (Met-O), using
CC respiratory chain electrons. Thus protects these proteins from
CC oxidative-stress damage caused by reactive species of oxygen and
CC chlorine generated by the host defense mechanisms. MsrPQ is essential
CC for the maintenance of envelope integrity under bleach stress, rescuing
CC a wide series of structurally unrelated periplasmic proteins from
CC methionine oxidation. The catalytic subunit MsrP is non-stereospecific,
CC being able to reduce both (R-) and (S-) diastereoisomers of methionine
CC sulfoxide. {ECO:0000255|HAMAP-Rule:MF_01206}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H2O + L-methionyl-[protein] = a quinol + L-
CC methionyl-(S)-S-oxide-[protein]; Xref=Rhea:RHEA:51292, Rhea:RHEA-
CC COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:24646, ChEBI:CHEBI:44120,
CC ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01206};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + H2O + L-methionyl-[protein] = a quinol + L-
CC methionyl-(R)-S-oxide-[protein]; Xref=Rhea:RHEA:51296, Rhea:RHEA-
CC COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:24646, ChEBI:CHEBI:45764,
CC ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01206};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01206};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01206};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit (MsrP) and a heme-binding
CC subunit (MsrQ). {ECO:0000255|HAMAP-Rule:MF_01206}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_01206}.
CC Note=Is attached to the inner membrane when interacting with the MsrQ
CC subunit. {ECO:0000255|HAMAP-Rule:MF_01206}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC {ECO:0000255|HAMAP-Rule:MF_01206}.
CC -!- SIMILARITY: Belongs to the MsrP family. {ECO:0000255|HAMAP-
CC Rule:MF_01206}.
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DR EMBL; CP000826; ABV43508.1; -; Genomic_DNA.
DR RefSeq; WP_012147109.1; NC_009832.1.
DR AlphaFoldDB; A8GK68; -.
DR SMR; A8GK68; -.
DR STRING; 399741.Spro_4414; -.
DR EnsemblBacteria; ABV43508; ABV43508; Spro_4414.
DR KEGG; spe:Spro_4414; -.
DR eggNOG; COG2041; Bacteria.
DR HOGENOM; CLU_045520_0_0_6; -.
DR OMA; WPYTEGL; -.
DR OrthoDB; 1729032at2; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016672; F:oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.420.10; -; 1.
DR HAMAP; MF_01206; MsrP; 1.
DR InterPro; IPR022867; MsrP.
DR InterPro; IPR000572; OxRdtase_Mopterin-bd_dom.
DR InterPro; IPR036374; OxRdtase_Mopterin-bd_sf.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF00174; Oxidored_molyb; 1.
DR SUPFAM; SSF56524; SSF56524; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding; Molybdenum; Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..43
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT CHAIN 44..333
FT /note="Protein-methionine-sulfoxide reductase catalytic
FT subunit MsrP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT /id="PRO_5000279787"
FT BINDING 87
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 90..91
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 145
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 180
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 232
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 237
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
FT BINDING 248..250
FT /ligand="Mo-molybdopterin"
FT /ligand_id="ChEBI:CHEBI:71302"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01206"
SQ SEQUENCE 333 AA; 37551 MW; 41D4587D4E2962F5 CRC64;
MSKQRKLTEA DVTPESVFYQ RRKVLQALGI TAASLALPHN AQADLLSWFK GNDRPKAPPG
KPLEFSKPAA WQAQLDLTPE DKVTGYNNFY EFGLDKADPA ANAGGLKTEG WQVRIDGEVA
KPITLDIDDL IKRFPLEQRI YRMRCVEAWS MVVPWIGFEL GKLIKFAEPN SNARYVAFQT
LYDPEQMPGQ KDRFIGGGLK YPYVEGLRLD EAMNPLALLT VGVYGKTLPP QNGAPLRLIT
PWKYGFKGIK SIVHIRLVRD QPPTTWNQSA PNEYGFYANV NPHVDHPRWS QATERFIGSG
GILDVKRQPT LLFNGYAEQV ASLYRGLDLR ENF
